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Editorial: Advances in Aspergillus fumigatus Pathobiology.

Frontiers in microbiology

Lamoth F, Juvvadi PR, Steinbach WJ.
PMID: 26870009
Front Microbiol. 2016 Feb 03;7:43. doi: 10.3389/fmicb.2016.00043. eCollection 2016.

No abstract available.

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Lamoth F, Juvvadi PR, Steinbach WJ. Editorial: Advances in Aspergillus fumigatus Pathobiology. Front Microbiol. 2016;7:43doi: 10.3389/fmicb.2016.00043.
Lamoth, F., Juvvadi, P. R., & Steinbach, W. J. (2016). Editorial: Advances in Aspergillus fumigatus Pathobiology. Frontiers in microbiology, 743. https://doi.org/10.3389/fmicb.2016.00043
Lamoth, Frédéric, et al. "Editorial: Advances in Aspergillus fumigatus Pathobiology." Frontiers in microbiology vol. 7 (2016): 43. doi: https://doi.org/10.3389/fmicb.2016.00043
Lamoth F, Juvvadi PR, Steinbach WJ. Editorial: Advances in Aspergillus fumigatus Pathobiology. Front Microbiol. 2016 Feb 03;7:43. doi: 10.3389/fmicb.2016.00043. eCollection 2016. PMID: 26870009; PMCID: PMC4737919.
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Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin.

Frontiers in molecular biosciences

Ley K, Christofferson A, Penna M, Winkler D, Maclaughlin S, Yarovsky I.
PMID: 26636091
Front Mol Biosci. 2015 Nov 16;2:64. doi: 10.3389/fmolb.2015.00064. eCollection 2015.

The class I hydrophobin EAS is part of a family of small, amphiphilic fungal proteins best known for their ability to self-assemble into stable monolayers that modify the hydrophobicity of a surface to facilitate further microbial growth. These proteins...

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Ley K, Christofferson A, Penna M, et al. Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin. Front Mol Biosci. 2015;2:64doi: 10.3389/fmolb.2015.00064.
Ley, K., Christofferson, A., Penna, M., Winkler, D., Maclaughlin, S., & Yarovsky, I. (2015). Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin. Frontiers in molecular biosciences, 264. https://doi.org/10.3389/fmolb.2015.00064
Ley, Kamron, et al. "Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin." Frontiers in molecular biosciences vol. 2 (2015): 64. doi: https://doi.org/10.3389/fmolb.2015.00064
Ley K, Christofferson A, Penna M, Winkler D, Maclaughlin S, Yarovsky I. Surface-water Interface Induces Conformational Changes Critical for Protein Adsorption: Implications for Monolayer Formation of EAS Hydrophobin. Front Mol Biosci. 2015 Nov 16;2:64. doi: 10.3389/fmolb.2015.00064. eCollection 2015. PMID: 26636091; PMCID: PMC4644811.
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Proteomic Analysis of Pathogenic Fungi Reveals Highly Expressed Conserved Cell Wall Proteins.

Journal of fungi (Basel, Switzerland)

Champer J, Ito JI, Clemons KV, Stevens DA, Kalkum M.
PMID: 26878023
J Fungi (Basel). 2016 Mar;2(1). doi: 10.3390/jof2010006. Epub 2016 Jan 12.

We are presenting a quantitative proteomics tally of the most commonly expressed conserved fungal proteins of the cytosol, the cell wall, and the secretome. It was our goal to identify fungi-typical proteins that do not share significant homology with...

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Champer J, Ito JI, Clemons KV, et al. Proteomic Analysis of Pathogenic Fungi Reveals Highly Expressed Conserved Cell Wall Proteins. J Fungi (Basel). 2016;2(1)doi: 10.3390/jof2010006.
Champer, J., Ito, J. I., Clemons, K. V., Stevens, D. A., & Kalkum, M. (2016). Proteomic Analysis of Pathogenic Fungi Reveals Highly Expressed Conserved Cell Wall Proteins. Journal of fungi (Basel, Switzerland), 2(1), . https://doi.org/10.3390/jof2010006
Champer, Jackson, et al. "Proteomic Analysis of Pathogenic Fungi Reveals Highly Expressed Conserved Cell Wall Proteins." Journal of fungi (Basel, Switzerland) vol. 2,1 (2016). doi: https://doi.org/10.3390/jof2010006
Champer J, Ito JI, Clemons KV, Stevens DA, Kalkum M. Proteomic Analysis of Pathogenic Fungi Reveals Highly Expressed Conserved Cell Wall Proteins. J Fungi (Basel). 2016 Mar;2(1). doi: 10.3390/jof2010006. Epub 2016 Jan 12. PMID: 26878023; PMCID: PMC4747415.
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Properties of Rhizopus stolonifer Polygalacturonase, an Elicitor of Casbene Synthetase Activity in Castor Bean (Ricinus communis L.) Seedlings.

Plant physiology

Lee SC, West CA.
PMID: 16661729
Plant Physiol. 1981 Apr;67(4):640-5. doi: 10.1104/pp.67.4.640.

Some properties of the polygalacturonase-elicitor from the filtrates of Rhizopus stolonifer cultures have been examined in an attempt to understand its mode of action as an elicitor of casbene synthetase activity in castor bean seedlings. Both the polygalacturonase activity...

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Lee SC, West CA. Properties of Rhizopus stolonifer Polygalacturonase, an Elicitor of Casbene Synthetase Activity in Castor Bean (Ricinus communis L.) Seedlings. Plant Physiol. 1981;67(4):640-5doi: 10.1104/pp.67.4.640.
Lee, S. C., & West, C. A. (1981). Properties of Rhizopus stolonifer Polygalacturonase, an Elicitor of Casbene Synthetase Activity in Castor Bean (Ricinus communis L.) Seedlings. Plant physiology, 67(4), 640-5. https://doi.org/10.1104/pp.67.4.640
Lee, S C, and West, C A. "Properties of Rhizopus stolonifer Polygalacturonase, an Elicitor of Casbene Synthetase Activity in Castor Bean (Ricinus communis L.) Seedlings." Plant physiology vol. 67,4 (1981): 640-5. doi: https://doi.org/10.1104/pp.67.4.640
Lee SC, West CA. Properties of Rhizopus stolonifer Polygalacturonase, an Elicitor of Casbene Synthetase Activity in Castor Bean (Ricinus communis L.) Seedlings. Plant Physiol. 1981 Apr;67(4):640-5. doi: 10.1104/pp.67.4.640. PMID: 16661729; PMCID: PMC425747.
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In silico analysis for transcription factors with Zn(II)(2)C(6) binuclear cluster DNA-binding domains in Candida albicans.

Comparative and functional genomics

Maicas S, Moreno I, Nieto A, Gómez M, Sentandreu R, Valentín E.
PMID: 18629206
Comp Funct Genomics. 2005;6(7):345-56. doi: 10.1002/cfg.492.

A total of 6047 open reading frames in the Candida albicans genome were screened for Zn(II)(2)C(6)-type zinc cluster proteins (or binuclear cluster proteins) involved in DNA recognition. These fungal proteins are transcription regulators of genes involved in a wide...

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Maicas S, Moreno I, Nieto A, et al. In silico analysis for transcription factors with Zn(II)(2)C(6) binuclear cluster DNA-binding domains in Candida albicans. Comp Funct Genomics. 2005;6(7):345-56doi: 10.1002/cfg.492.
Maicas, S., Moreno, I., Nieto, A., Gómez, M., Sentandreu, R., & Valentín, E. (2005). In silico analysis for transcription factors with Zn(II)(2)C(6) binuclear cluster DNA-binding domains in Candida albicans. Comparative and functional genomics, 6(7), 345-56. https://doi.org/10.1002/cfg.492
Maicas, Sergi, et al. "In silico analysis for transcription factors with Zn(II)(2)C(6) binuclear cluster DNA-binding domains in Candida albicans." Comparative and functional genomics vol. 6,7 (2005): 345-56. doi: https://doi.org/10.1002/cfg.492
Maicas S, Moreno I, Nieto A, Gómez M, Sentandreu R, Valentín E. In silico analysis for transcription factors with Zn(II)(2)C(6) binuclear cluster DNA-binding domains in Candida albicans. Comp Funct Genomics. 2005;6(7):345-56. doi: 10.1002/cfg.492. PMID: 18629206; PMCID: PMC2447501.
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An Improved Method for Protein Extraction from Minuscule Quantities of Fungal Biomass.

Indian journal of microbiology

Krishnaswamy A, Barnes N, Lotlikar NP, Damare SR.
PMID: 30728637
Indian J Microbiol. 2019 Mar;59(1):100-104. doi: 10.1007/s12088-018-0752-y. Epub 2018 Jun 26.

Filamentous fungi are ubiquitous eukaryotes having chitin as a major constituent of the cell wall. Chitin is tough to lyse due to which the intracellular fungal proteins are not readily accessible. The problem is further enhanced when the biomass...

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Krishnaswamy A, Barnes N, Lotlikar NP, et al. An Improved Method for Protein Extraction from Minuscule Quantities of Fungal Biomass. Indian J Microbiol. 2018;59(1):100-104doi: 10.1007/s12088-018-0752-y.
Krishnaswamy, A., Barnes, N., Lotlikar, N. P., & Damare, S. R. (2019). An Improved Method for Protein Extraction from Minuscule Quantities of Fungal Biomass. Indian journal of microbiology, 59(1), 100-104. https://doi.org/10.1007/s12088-018-0752-y
Krishnaswamy, Akhila, et al. "An Improved Method for Protein Extraction from Minuscule Quantities of Fungal Biomass." Indian journal of microbiology vol. 59,1 (2019): 100-104. doi: https://doi.org/10.1007/s12088-018-0752-y
Krishnaswamy A, Barnes N, Lotlikar NP, Damare SR. An Improved Method for Protein Extraction from Minuscule Quantities of Fungal Biomass. Indian J Microbiol. 2019 Mar;59(1):100-104. doi: 10.1007/s12088-018-0752-y. Epub 2018 Jun 26. PMID: 30728637; PMCID: PMC6328415.
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Structure Formation in Class I and Class II Hydrophobins at the Air-Water Interface under Multiple Compression/Expansion Cycles.

ChemistryOpen

Kordts M, Kampe M, Kerth A, Hinderberger D.
PMID: 30524926
ChemistryOpen. 2018 Nov 21;7(12):1005-1013. doi: 10.1002/open.201800176. eCollection 2018 Dec.

Hydrophobins are small amphiphilic fungal proteins empirically divided into two classes. We investigated the self-assembled structures of class I SC3 from

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Kordts M, Kampe M, Kerth A, et al. Structure Formation in Class I and Class II Hydrophobins at the Air-Water Interface under Multiple Compression/Expansion Cycles. ChemistryOpen. 2018;7(12):1005-1013doi: 10.1002/open.201800176.
Kordts, M., Kampe, M., Kerth, A., & Hinderberger, D. (2018). Structure Formation in Class I and Class II Hydrophobins at the Air-Water Interface under Multiple Compression/Expansion Cycles. ChemistryOpen, 7(12), 1005-1013. https://doi.org/10.1002/open.201800176
Kordts, Martin, et al. "Structure Formation in Class I and Class II Hydrophobins at the Air-Water Interface under Multiple Compression/Expansion Cycles." ChemistryOpen vol. 7,12 (2018): 1005-1013. doi: https://doi.org/10.1002/open.201800176
Kordts M, Kampe M, Kerth A, Hinderberger D. Structure Formation in Class I and Class II Hydrophobins at the Air-Water Interface under Multiple Compression/Expansion Cycles. ChemistryOpen. 2018 Nov 21;7(12):1005-1013. doi: 10.1002/open.201800176. eCollection 2018 Dec. PMID: 30524926; PMCID: PMC6276105.
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Transcriptome sequencing and screening of genes related to glucose availability in Schizosaccharomyces pombe by RNA-seq analysis.

Genetics and molecular biology

Tarhan Ç, Çakır Ö.
PMID: 34460892
Genet Mol Biol. 2021 Aug 27;44(3):e20200245. doi: 10.1590/1678-4685-GMB-2020-0245. eCollection 2021.

While calorie restriction is the most used experimental intervention to increase lifespan in numerous model organisms, increasing evidence suggests that excess glucose leads to decreased lifespan in various organisms. To fully understand the molecular basis of the pro-aging effect...

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Tarhan Ç, Çakır Ö. Transcriptome sequencing and screening of genes related to glucose availability in Schizosaccharomyces pombe by RNA-seq analysis. Genet Mol Biol. 2021;44(3):e20200245doi: 10.1590/1678-4685-GMB-2020-0245.
Tarhan, �. �., & Çakır, �. �. (2021). Transcriptome sequencing and screening of genes related to glucose availability in Schizosaccharomyces pombe by RNA-seq analysis. Genetics and molecular biology, 44(3), e20200245. https://doi.org/10.1590/1678-4685-GMB-2020-0245
Tarhan, Çağatay, and Çakır, Özgür. "Transcriptome sequencing and screening of genes related to glucose availability in Schizosaccharomyces pombe by RNA-seq analysis." Genetics and molecular biology vol. 44,3 (2021): e20200245. doi: https://doi.org/10.1590/1678-4685-GMB-2020-0245
Tarhan Ç, Çakır Ö. Transcriptome sequencing and screening of genes related to glucose availability in Schizosaccharomyces pombe by RNA-seq analysis. Genet Mol Biol. 2021 Aug 27;44(3):e20200245. doi: 10.1590/1678-4685-GMB-2020-0245. eCollection 2021. PMID: 34460892; PMCID: PMC8404550.
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Sub-Lethal Effects of Partially Purified Protein Extracted from .

Insects

Keerio AU, Nazir T, Anwar T, Zeeshan Majeed M, Abdulle YA, Jatoi GH, Gadhi MA, Qiu D.
PMID: 32867017
Insects. 2020 Aug 27;11(9). doi: 10.3390/insects11090574.

Plants rely on various physiological and molecular defense mechanisms against biotic stresses such as herbivore insects. Many entomopathogenic fungi synthesize protein molecules that can trigger these plant defenses. This laboratory study characterized the bioactivity of a partially purified protein...

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Keerio AU, Nazir T, Anwar T, et al. Sub-Lethal Effects of Partially Purified Protein Extracted from . Insects. 2020;11(9)doi: 10.3390/insects11090574.
Keerio, A. U., Nazir, T., Anwar, T., Zeeshan Majeed, M., Abdulle, Y. A., Jatoi, G. H., Gadhi, M. A., & Qiu, D. (2020). Sub-Lethal Effects of Partially Purified Protein Extracted from . Insects, 11(9), . https://doi.org/10.3390/insects11090574
Keerio, Azhar Uddin, et al. "Sub-Lethal Effects of Partially Purified Protein Extracted from ." Insects vol. 11,9 (2020). doi: https://doi.org/10.3390/insects11090574
Keerio AU, Nazir T, Anwar T, Zeeshan Majeed M, Abdulle YA, Jatoi GH, Gadhi MA, Qiu D. Sub-Lethal Effects of Partially Purified Protein Extracted from . Insects. 2020 Aug 27;11(9). doi: 10.3390/insects11090574. PMID: 32867017; PMCID: PMC7564989.
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Taxonomically Restricted Wheat Genes Interact With Small Secreted Fungal Proteins and Enhance Resistance to Septoria Tritici Blotch Disease.

Frontiers in plant science

Brennan CJ, Zhou B, Benbow HR, Ajaz S, Karki SJ, Hehir JG, O'Driscoll A, Feechan A, Mullins E, Doohan FM.
PMID: 32477375
Front Plant Sci. 2020 May 07;11:433. doi: 10.3389/fpls.2020.00433. eCollection 2020.

Understanding the nuances of host/pathogen interactions are paramount if we wish to effectively control cereal diseases. In the case of the wheat/

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Brennan CJ, Zhou B, Benbow HR, et al. Taxonomically Restricted Wheat Genes Interact With Small Secreted Fungal Proteins and Enhance Resistance to Septoria Tritici Blotch Disease. Front Plant Sci. 2020;11:433doi: 10.3389/fpls.2020.00433.
Brennan, C. J., Zhou, B., Benbow, H. R., Ajaz, S., Karki, S. J., Hehir, J. G., O'Driscoll, A., Feechan, A., Mullins, E., & Doohan, F. M. (2020). Taxonomically Restricted Wheat Genes Interact With Small Secreted Fungal Proteins and Enhance Resistance to Septoria Tritici Blotch Disease. Frontiers in plant science, 11433. https://doi.org/10.3389/fpls.2020.00433
Brennan, Ciarán J, et al. "Taxonomically Restricted Wheat Genes Interact With Small Secreted Fungal Proteins and Enhance Resistance to Septoria Tritici Blotch Disease." Frontiers in plant science vol. 11 (2020): 433. doi: https://doi.org/10.3389/fpls.2020.00433
Brennan CJ, Zhou B, Benbow HR, Ajaz S, Karki SJ, Hehir JG, O'Driscoll A, Feechan A, Mullins E, Doohan FM. Taxonomically Restricted Wheat Genes Interact With Small Secreted Fungal Proteins and Enhance Resistance to Septoria Tritici Blotch Disease. Front Plant Sci. 2020 May 07;11:433. doi: 10.3389/fpls.2020.00433. eCollection 2020. PMID: 32477375; PMCID: PMC7236048.
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Different Hydrophobins of .

Frontiers in microbiology

Quarantin A, Hadeler B, Kröger C, Schäfer W, Favaron F, Sella L, Martínez-Rocha AL.
PMID: 31031728
Front Microbiol. 2019 Apr 12;10:751. doi: 10.3389/fmicb.2019.00751. eCollection 2019.

Hydrophobins (HPs) are small secreted fungal proteins possibly involved in several processes such as formation of fungal aerial structures, attachment to hydrophobic surfaces, interaction with the environment and protection against the host defense system. The genome of the necrotrophic...

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Quarantin A, Hadeler B, Kröger C, et al. Different Hydrophobins of . Front Microbiol. 2019;10:751doi: 10.3389/fmicb.2019.00751.
Quarantin, A., Hadeler, B., Kröger, C., Schäfer, W., Favaron, F., Sella, L., & Martínez-Rocha, A. L. (2019). Different Hydrophobins of . Frontiers in microbiology, 10751. https://doi.org/10.3389/fmicb.2019.00751
Quarantin, Alessandra, et al. "Different Hydrophobins of ." Frontiers in microbiology vol. 10 (2019): 751. doi: https://doi.org/10.3389/fmicb.2019.00751
Quarantin A, Hadeler B, Kröger C, Schäfer W, Favaron F, Sella L, Martínez-Rocha AL. Different Hydrophobins of . Front Microbiol. 2019 Apr 12;10:751. doi: 10.3389/fmicb.2019.00751. eCollection 2019. PMID: 31031728; PMCID: PMC6474331.
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The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor.

Biotechnology for biofuels

Pereira EO, Tsang A, McAllister TA, Menassa R.
PMID: 23915965
Biotechnol Biofuels. 2013 Aug 01;6:111. doi: 10.1186/1754-6834-6-111. eCollection 2013.

BACKGROUND: Microorganisms are the most proficient decomposers in nature, using secreted enzymes in the hydrolysis of lignocellulose. As such, they present the most abundant source for discovery of new enzymes. Acremonium alcalophilum is the only known cellulolytic fungus that...

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Pereira EO, Tsang A, McAllister TA, et al. The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor. Biotechnol Biofuels. 2013;6:111doi: 10.1186/1754-6834-6-111.
Pereira, E. O., Tsang, A., McAllister, T. A., & Menassa, R. (2013). The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor. Biotechnology for biofuels, 6111. https://doi.org/10.1186/1754-6834-6-111
Pereira, Eridan Orlando, et al. "The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor." Biotechnology for biofuels vol. 6 (2013): 111. doi: https://doi.org/10.1186/1754-6834-6-111
Pereira EO, Tsang A, McAllister TA, Menassa R. The production and characterization of a new active lipase from Acremonium alcalophilum using a plant bioreactor. Biotechnol Biofuels. 2013 Aug 01;6:111. doi: 10.1186/1754-6834-6-111. eCollection 2013. PMID: 23915965; PMCID: PMC3750315.
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Showing 1 to 12 of 31 entries